5AEY
actin-like ParM protein bound to AMPPNP
Summary for 5AEY
| Entry DOI | 10.2210/pdb5aey/pdb |
| EMDB information | 2850 |
| Descriptor | PLASMID SEGREGATION PROTEIN PARM, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (2 entities in total) |
| Functional Keywords | structural protein, bacterial cytoskeleton, plasmid segregation, actin- like protein |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 5 |
| Total formula weight | 180697.10 |
| Authors | Bharat, T.A.M.,Murshudov, G.N.,Sachse, C.,Lowe, J. (deposition date: 2015-01-12, release date: 2015-04-22, Last modification date: 2024-05-08) |
| Primary citation | Bharat, T.A.M.,Murshudov, G.N.,Sachse, C.,Lowe, J. Structures of Actin-Like Parm Filaments Show Architecture of Plasmid-Segregating Spindles. Nature, 523:106-, 2015 Cited by PubMed Abstract: Active segregation of Escherichia coli low-copy-number plasmid R1 involves formation of a bipolar spindle made of left-handed double-helical actin-like ParM filaments. ParR links the filaments with centromeric parC plasmid DNA, while facilitating the addition of subunits to ParM filaments. Growing ParMRC spindles push sister plasmids to the cell poles. Here, using modern electron cryomicroscopy methods, we investigate the structures and arrangements of ParM filaments in vitro and in cells, revealing at near-atomic resolution how subunits and filaments come together to produce the simplest known mitotic machinery. To understand the mechanism of dynamic instability, we determine structures of ParM filaments in different nucleotide states. The structure of filaments bound to the ATP analogue AMPPNP is determined at 4.3 Å resolution and refined. The ParM filament structure shows strong longitudinal interfaces and weaker lateral interactions. Also using electron cryomicroscopy, we reconstruct ParM doublets forming antiparallel spindles. Finally, with whole-cell electron cryotomography, we show that doublets are abundant in bacterial cells containing low-copy-number plasmids with the ParMRC locus, leading to an asynchronous model of R1 plasmid segregation. PubMed: 25915019DOI: 10.1038/NATURE14356 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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